A monthly journal publishing high-quality, peer-reviewed research on all topics related to RNA and its metabolism in all organisms

This dataset compiles experimentally validated splice leader (SL) sequences from diverse eukaryotic taxa, providing a comparative reference for studies on trans-splicing and RNA processing. Version 7 represents a major update from v3 (January 2025), nearly doubling the number of entries from 112 to 210 sequences (+98 entries, +87%).Taxonomic coverage has been significantly expanded to now include 11 phyla: Euglenozoa, Nematoda, Platyhelminthes, Cnidaria, Rotifera, Chordata, Alveolata, and four newly added phyla — Arthropoda (Copepoda), Chaetognatha (Sagittoidea), Cryptista (Cryptomonada), and Ctenophora (Tentaculata/Nuda). The largest expansions were in Nematoda, Cnidaria, and Chaetognatha.The dataset schema was restructured to improve phylogenetic resolution, replacing the single "Family" field with a two-level "Phylum / Subgroup" classification. A formal SL sequence naming convention was introduced, with 170 of 210 entries carrying standardized identifiers. Each entry includes the SL sequence (5' to 3'), sequence length, primary literature reference (DOI and PMID), and contributor information.

This dataset compiles experimentally validated splice leader (SL) sequences from diverse eukaryotic taxa, providing a comparative reference for studies on trans-splicing and RNA processing. Version 7 represents a major update from v3 (January 2025), nearly doubling the number of entries from 112 to 210 sequences (+98 entries, +87%).Taxonomic coverage has been significantly expanded to now include 11 phyla: Euglenozoa, Nematoda, Platyhelminthes, Cnidaria, Rotifera, Chordata, Alveolata, and four newly added phyla — Arthropoda (Copepoda), Chaetognatha (Sagittoidea), Cryptista (Cryptomonada), and Ctenophora (Tentaculata/Nuda). The largest expansions were in Nematoda, Cnidaria, and Chaetognatha.The dataset schema was restructured to improve phylogenetic resolution, replacing the single "Family" field with a two-level "Phylum / Subgroup" classification. A formal SL sequence naming convention was introduced, with 170 of 210 entries carrying standardized identifiers. Each entry includes the SL sequence (5' to 3'), sequence length, primary literature reference (DOI and PMID), and contributor information.

A monthly journal publishing high-quality, peer-reviewed research on all topics related to RNA and its metabolism in all organisms

Glucose catabolism in trypanosomatids differs significantly from that in most other eukaryotes. Here, the first few enzymes of the pathway are all located inside glycosomes, that is, the peroxisome-like microbodies uniquely present in the Kinetoplastida and Diplonemida of the Euglenozoa. Glycosomal AMP/ADP/ATP and NAD(H)^(+) pools cannot freely equilibrate with their corresponding cytosolic pools, and any ATP and NAD^(+) consumed within the organelles have to be regenerated inside to maintain...

Heterotrimeric kinesin 2 is the canonical motor protein for anterograde intraflagellar transport (IFT), driving movement of protein complexes towards the tip of cilia and flagella. Here, we show that all members of the Euglenozoa group lack genes for heterotrimeric kinesins and instead possess a variable number of genes for two homodimeric kinesins termed KIN2A and KIN2B. When expressed in vitro, both Trypanosoma brucei kinesins form homodimers and move processively along brain microtubules, KIN2A being faster than KIN2B. Studies in T. brucei and Leishmania mexicana show anterograde and retrograde IFT of both kinesins, with KIN2A travelling throughout the whole length of the flagellum, while KIN2B is concentrated at its base. In the proximal portion of the flagellum, most KIN2B molecules travel without IFT proteins, except for a few particles that are associated with IFT proteins and reach the tip. Surprisingly, the absence of KIN2A has mild effects on IFT and flagellum assembly, whereas KIN2B is essential for both. Investigation of trypanosome flagella deprived of KIN2B revealed that IFT proteins do not access these flagella but that KIN2A can still circulate. These results support a division-of-labour model where KIN2B is responsible for the import of IFT proteins while KIN2A is responsible for most of the anterograde transport.

Heterotrimeric kinesin 2 is the canonical motor protein for anterograde intraflagellar transport (IFT), driving movement of protein complexes towards the tip of cilia and flagella. Here, we show that all members of the Euglenozoa group lack genes for heterotrimeric kinesins and instead possess a variable number of genes for two homodimeric kinesins termed KIN2A and KIN2B. When expressed in vitro, both Trypanosoma brucei kinesins form homodimers and move processively along brain microtubules, KIN2A being faster than KIN2B. Studies in T. brucei and Leishmania mexicana show anterograde and retrograde IFT of both kinesins, with KIN2A travelling throughout the whole length of the flagellum, while KIN2B is concentrated at its base. In the proximal portion of the flagellum, most KIN2B molecules travel without IFT proteins, except for a few particles that are associated with IFT proteins and reach the tip. Surprisingly, the absence of KIN2A has mild effects on IFT and flagellum assembly, whereas KIN2B is essential for both. Investigation of trypanosome flagella deprived of KIN2B revealed that IFT proteins do not access these flagella but that KIN2A can still circulate. These results support a division-of-labour model where KIN2B is responsible for the import of IFT proteins while KIN2A is responsible for most of the anterograde transport.

Cristae enclose respiratory chain complexes, making them the bioenergetic subcompartments of mitochondria. The MICOS complex is among the inducers of membrane curvature needed for crista formation. Resembling the respiratory chain complexes, MICOS is organized around a core protein, the mitofilin-domain bearing Mic60, that was inherited from the alphaproteobacterial progenitor of mitochondria. Extant alphaproteobacteria express Mic60 to form their own bioenergetic subcompartments, demonstrating...

PEX19 is a cytosolic receptor that directs membrane proteins post-translationally to peroxisomes, as well as to mitochondria, lipid droplets, and the endoplasmic reticulum. A comprehensive Trypanosoma PEX19 interactome analysis uncovered PEX38 as a novel and essential Euglenozoa-specific peroxin. PEX38 contains distinct domains that bind the co-chaperone Hip and the PEX3-binding motif of PEX19, suggesting a role in stabilizing membrane protein and preventing premature membrane docking. PEX38 illustrates functional repurposing in organelle biogenesis. It originated from a remnant of the GET/TRC pathway, typically responsible for the targeting of tail-anchored proteins to the endoplasmic reticulum. While most components of this machinery are absent in Euglenozoa, PEX38 has been retained and adapted to mediate peroxisomal membrane protein targeting. This evolutionary adaptation is unique to Euglenozoa. Because the PEX19-PEX38 interaction is essential for parasite viability and PEX38 has no human homologs, this complex is a promising therapeutic target against trypanosomatid parasites.

PEX19 is a cytosolic receptor that directs membrane proteins post-translationally to peroxisomes, as well as to mitochondria, lipid droplets, and the endoplasmic reticulum. A comprehensive Trypanosoma PEX19 interactome analysis uncovered PEX38 as a novel and essential Euglenozoa-specific peroxin. PEX38 contains distinct domains that bind the co-chaperone Hip and the PEX3-binding motif of PEX19, suggesting a role in stabilizing membrane protein and preventing premature membrane docking. PEX38 illustrates functional repurposing in organelle biogenesis. It originated from a remnant of the GET/TRC pathway, typically responsible for the targeting of tail-anchored proteins to the endoplasmic reticulum. While most components of this machinery are absent in Euglenozoa, PEX38 has been retained and adapted to mediate peroxisomal membrane protein targeting. This evolutionary adaptation is unique to Euglenozoa. Because the PEX19-PEX38 interaction is essential for parasite viability and PEX38 has no human homologs, this complex is a promising therapeutic target against trypanosomatid parasites.

Abstract. Cristae enclose respiratory chain complexes, making them the bioenergetic subcompartments of mitochondria. The Mitochondrial contact site and Cri

Metabolomics, the comprehensive study of low-molecular-weight metabolites, provides a direct snapshot of an organism’s physiological state and complements genomics and proteomics. Ion mobility (...